Ménez A, Bouet F, Guschlbauer W, Fromageot P
Biochemistry. 1980 Sep 2;19(18):4166-72. doi: 10.1021/bi00559a005.
The four disulfide bonds of nine homologous short curare-like polypeptides are cleaved by reduced dithiothreitol. Air oxidation renaturations of the reduced compounds are followed by far-ultraviolet circular dichroism analysis, and the kinetics of refolding thus determined are compared. They indicate that three toxins refold 4--10 times more slowly than the six others. It is shown that a significant difference between the refolding kinetics still subsists when renaturations are made in the presence of various concentrations of thiol-disulfide exchange reagents or at various pH values. From an examination of the toxin sequences, it is proposed that a single additional amino acid insertion is responsible for the difference in the observed kinetics. This proposal is supported by temperature studies of renaturation kinetics.
九种同源的箭毒样短多肽的四条二硫键被还原型二硫苏糖醇裂解。通过远紫外圆二色性分析跟踪还原化合物的空气氧化复性过程，并比较由此确定的复性动力学。结果表明，三种毒素的复性速度比其他六种慢4至10倍。研究表明，当在不同浓度的硫醇-二硫键交换试剂存在下或在不同pH值下进行复性时，复性动力学之间的显著差异仍然存在。通过对毒素序列的研究，提出一个额外的氨基酸插入是观察到的动力学差异的原因。复性动力学的温度研究支持了这一观点。
